sRANKL Mouse
Greater than 95.0% as determined by SDS-PAGE.
Description
sRANKL Mouse Recombinant produced in E.coli is single, non-glycosylated, polypeptide chain containing 174 amino acids ( 143-316 a.a.) and having a total molecular mass of 19.9kDa. CD254 is purified by proprietary chromatographic techniques.
Product Specs
Recombinant mouse sRANKL, a non-glycosylated polypeptide chain consisting of 174 amino acids (143-316 a.a.), is produced in E. coli. With a molecular weight of 19.9 kDa, this protein variant undergoes purification using proprietary chromatographic techniques to isolate the CD254 molecule.
This protein solution (1mg/ml) is lyophilized in a buffer of 10mM Na2PO4 at pH 7.5 and 50mM NaCl.
To reconstitute the lyophilized sRANKL, it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration of at least 100µg/ml. The resulting solution can be further diluted in other aqueous solutions as needed.
Lyophilized TNFSF11 can be stored at room temperature for up to 3 weeks, but for extended storage, it should be kept desiccated at a temperature below -18°C. After reconstitution, sRANKL should be stored at 4°C for no more than 2-7 days. For long-term storage, it is advisable to add a carrier protein such as HSA or BSA (0.1%) and avoid repeated freeze-thaw cycles.
The purity of this product is determined to be greater than 95.0% based on SDS-PAGE analysis.
The biological activity of this product is assessed based on its capacity to induce osteoclast formation in murine RAW264.7 cells. Using a concentration of 50ng/ml, this activity is demonstrated in a study titled "Corning® Osteo Assay Surface 24 Well Plates with Transwell® Permeable Supports- A Useful Tool for Co-Culture Studies" by Rebecca M. Wood and Mark Rothenber. This corresponds to a specific activity of 20,000 Units/mg.
PAMMEGSWLD VAQRGKPEAQ PFAHLTINAA SIPSGSHKVT LSSWYHDRGW AKISNMTLSN GKLRVNQDGF YYLYANICFR HHETSGSVPT DYLQLMVYVV KTSIKIPSSH NLMKGGSTKN WSGNSEFHFY SINVGGFFKL RAGEEISIQV SNPSLLDPDQ DATYFGAFKV QDID.
Product Science Overview
RANKL is a type II transmembrane protein with an extracellular domain at the carboxy-terminus . This ectodomain can be cleaved by enzymes such as matrix metalloproteinases, releasing a soluble form of RANKL into the extracellular environment . The soluble form of RANKL is often used in research and therapeutic applications due to its ability to interact with its receptor, RANK, on the surface of target cells.
RANKL is expressed in several tissues and cell types, including fibroblasts, T cells, and osteoblasts . It plays a significant role in the differentiation and activation of osteoclasts, which are cells responsible for bone resorption . Additionally, RANKL is involved in the maturation of dendritic cells and the regulation of T cell-dependent immune responses .
The primary function of RANKL is to bind to its receptor, RANK, which is expressed on the surface of osteoclast precursors and mature osteoclasts . This binding triggers a signaling cascade that leads to the differentiation, activation, and survival of osteoclasts . Osteoclasts are essential for bone remodeling, a process that maintains bone health by balancing bone formation and resorption.
RANKL also interacts with osteoprotegerin (OPG), a decoy receptor that inhibits the binding of RANKL to RANK . This interaction prevents osteoclastogenesis and leads to the accumulation of bone and cartilage . High expression of RANKL is observed during degenerative bone diseases and in tumors, highlighting its role in pathological conditions .
Recombinant mouse RANKL, particularly its soluble form, is widely used in research to study bone metabolism, immune cell activation, and tumor growth . It is also utilized in differentiation studies and functional assays involving osteoclasts and other cell types . The recombinant protein is typically produced in bacterial expression systems, such as Escherichia coli, and is purified to high standards for use in various experimental applications .
